Structure of PDB 1lyc Chain A

Receptor sequence
>1lycA (length=336) Species: 5346 (Coprinopsis cinerea) [Search protein sequence]
SVTCPGGQSTSNSQCCVWFDVLDDLQTNFYQGSKCESPVRKILRIVFHDA
IGFSPALTAAGQFGGGGADGSIIAHSNIELAFPANGGLTDTVEALRAVGI
NHGVSFGDLIQFATAVGMSNCPGSPRLEFLTGRSSSSQPSPPSLIPGPGN
TVTAILDRMGDAGFSPDEVVDLLAAHSLASQEGLNSAIFRSPLDSTPQVF
DTQFYIETLLKGTTQPGPSLGFAEELSPFPGEFRMRSDALLARDSRTACR
WQSMTSSNEVMGQRYRAAMAKMSVLGFDRNALTDCSDVIPSAVSNNAAPV
IPGGLTVDDIEVSCPSEPFPEIAAASGPLPALAPAP
3D structure
PDB1lyc Impact of the physical and chemical environment on the molecular structure of Coprinus cinereus peroxidase.
ChainA
Resolution1.57 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R51 H55 H183 L200
Catalytic site (residue number reindexed from 1) R44 H48 H176 L193
Enzyme Commision number 1.11.1.7: peroxidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA A S184 D201 T203 V206 D208 S177 D194 T196 V199 D201
BS02 CA A D56 G74 D76 S78 D49 G67 D69 S71
BS03 HEM A R47 L50 R51 F54 G154 P155 L179 L180 A182 H183 A186 S187 Q188 E189 G190 L191 M242 M276 R40 L43 R44 F47 G147 P148 L172 L173 A175 H176 A179 S180 Q181 E182 G183 L184 M235 M269
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0140825 lactoperoxidase activity
Biological Process
GO:0000302 response to reactive oxygen species
GO:0006979 response to oxidative stress
GO:0034599 cellular response to oxidative stress
GO:0042744 hydrogen peroxide catabolic process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1lyc, PDBe:1lyc, PDBj:1lyc
PDBsum1lyc
PubMed12777760
UniProtP28314|PER_COPCI Peroxidase (Gene Name=CIP1)

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